Literature summary for 3.6.4.10 extracted from

Hawkins, T.A.; Haramis, A.; Etard, C.; Prodromou, C.; Vaughan, C.K.; Ashworth, R.; Ray, S.; Behra, M.; Holder, N.; Talbot, W.S.; Pearl, L.H.; Strahle, U.; Wilson, S.W.
The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis (2008), Development, 135, 1147-1156.

Search for more literature for 3.6.4.10

Protein Variants

Protein Variants	Comment	Organism
additional information	in slothu45 mutant, the initial steps in sarcomere assembly take place, but thick filaments are absent and filamentous I-Z-I brushes fail to align or adopt correct spacing. The mutation only affects skeletal muscle and mutant embryos show no other obvious phenotypes. Phenotype is due to mutation in one copy of a tandemly duplicated hsp90a gene disrupting the chaperoning function through interference with aTPase activity. Loss of Hsp90a function leads to the downregulation of genes encoding sarcomeric proteins and upregulation of hsp90a and several other genes encoding proteins that may act with Hsp90a during sarcomere assembly	Danio rerio

Organism

Organism	UniProt	Comment	Textmining
Danio rerio	-	isoform Hsp90a	-

Synonyms

Synonyms	Comment	Organism
Hsp90a	-	Danio rerio

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)